Carnosine protects against the inactivation of esterase induced by glycation and a steroid
Laboratory studyOther animals
- Design
- Laboratory study
- What was measured
- Esterase activity (p-nitrophenyl acetate assay) and electrophoretic cross-linking after incubation with fructose, fructose 6-phosphate, ribose or prednisolone-21-hemisuccinate, with and without carnosine.
What the authors reported
Esterase was progressively inactivated by the three sugars and more strongly by the steroid. Carnosine significantly inhibited inactivation by all four compounds and reduced cross-linking. The authors present this as further evidence of anti-glycation action and propose that carnosine may also act as an anti-steroid agent.
Limits of this study
Model enzyme in vitro. Abstract only.
Source
PubMed 15955455 · doi:10.1016/j.bbadis.2004.11.008
Entry checked against PubMed abstract (E-utilities) on 2026-10-19. The dose shown is the dose the researchers used. It is not a recommendation. How to read this page.